HEADER TRANSCRIPTION 30-MAY-13 4KZM
TITLE CRYSTAL STRUCTURE OF TR3 LBD S553A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 4 GROUP A MEMBER 1;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 351-598;
COMPND 5 SYNONYM: EARLY RESPONSE PROTEIN NAK1, NUCLEAR HORMONE RECEPTOR
COMPND 6 NUR/77, NUR77, ORPHAN NUCLEAR RECEPTOR HMR, ORPHAN NUCLEAR RECEPTOR
COMPND 7 TR3, ST-59, TESTICULAR RECEPTOR 3;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GFRP1, HMR, NAK1, NR4A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ORPHAN NUCLEAR RECEPTOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.LI,Q.ZHANG,A.LI,X.TIAN,Q.CAI,W.WANG,Y.WANG,H.CHEN,Y.XING,Q.WU,T.LIN
REVDAT 4 20-MAR-24 4KZM 1 REMARK
REVDAT 3 25-DEC-19 4KZM 1 JRNL SEQADV
REVDAT 2 15-NOV-17 4KZM 1 REMARK
REVDAT 1 18-DEC-13 4KZM 0
JRNL AUTH W.J.WANG,Y.WANG,H.Z.CHEN,Y.Z.XING,F.W.LI,Q.ZHANG,B.ZHOU,
JRNL AUTH 2 H.K.ZHANG,J.ZHANG,X.L.BIAN,L.LI,Y.LIU,B.X.ZHAO,Y.CHEN,R.WU,
JRNL AUTH 3 A.Z.LI,L.M.YAO,P.CHEN,Y.ZHANG,X.Y.TIAN,F.BEERMANN,M.WU,
JRNL AUTH 4 J.HAN,P.Q.HUANG,T.LIN,Q.WU
JRNL TITL ORPHAN NUCLEAR RECEPTOR TR3 ACTS IN AUTOPHAGIC CELL DEATH
JRNL TITL 2 VIA MITOCHONDRIAL SIGNALING PATHWAY.
JRNL REF NAT.CHEM.BIOL. V. 10 133 2014
JRNL REFN ESSN 1552-4469
JRNL PMID 24316735
JRNL DOI 10.1038/NCHEMBIO.1406
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 29888
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1544
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1799
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3618
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.79000
REMARK 3 B22 (A**2) : 1.72000
REMARK 3 B33 (A**2) : -2.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.253
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.591
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3707 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3678 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5016 ; 1.840 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8462 ; 1.291 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 458 ; 5.655 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 153 ;36.367 ;23.203
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 643 ;18.640 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;20.431 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 585 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4067 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 811 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4KZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000079994.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29916
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE, GLYCEROL, PH
REMARK 280 4.2, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.24050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.22150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.17250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.22150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.24050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.17250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 350
REMARK 465 SER B 351
REMARK 465 LYS B 352
REMARK 465 PRO B 353
REMARK 465 LYS B 354
REMARK 465 GLN B 355
REMARK 465 PRO B 356
REMARK 465 PRO B 357
REMARK 465 ASP B 358
REMARK 465 ALA B 359
REMARK 465 SER B 360
REMARK 465 HIS B 394
REMARK 465 PHE B 395
REMARK 465 GLY B 396
REMARK 465 GLY B 544
REMARK 465 GLU B 545
REMARK 465 PRO B 546
REMARK 465 GLN B 547
REMARK 465 PRO B 548
REMARK 465 LEU B 599
REMARK 465 GLU B 600
REMARK 465 HIS B 601
REMARK 465 HIS B 602
REMARK 465 HIS B 603
REMARK 465 HIS B 604
REMARK 465 HIS B 605
REMARK 465 HIS B 606
REMARK 465 MET A 350
REMARK 465 SER A 351
REMARK 465 LYS A 352
REMARK 465 PRO A 353
REMARK 465 LYS A 354
REMARK 465 GLN A 355
REMARK 465 PRO A 356
REMARK 465 PRO A 357
REMARK 465 ASP A 358
REMARK 465 ALA A 359
REMARK 465 SER A 360
REMARK 465 PRO A 361
REMARK 465 GLU A 545
REMARK 465 PRO A 546
REMARK 465 GLN A 547
REMARK 465 PRO A 548
REMARK 465 LEU A 599
REMARK 465 GLU A 600
REMARK 465 HIS A 601
REMARK 465 HIS A 602
REMARK 465 HIS A 603
REMARK 465 HIS A 604
REMARK 465 HIS A 605
REMARK 465 HIS A 606
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA B 362 CB
REMARK 470 LYS B 381 CG CD CE NZ
REMARK 470 GLN B 388 CD OE1 NE2
REMARK 470 LYS B 397 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CD1 ILE B 448 O HOH B 829 1.75
REMARK 500 OE1 GLU B 398 OE1 GLU B 579 1.86
REMARK 500 O HOH A 862 O HOH A 888 1.90
REMARK 500 N PRO B 361 N LEU B 364 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 475 CB CYS B 475 SG -0.133
REMARK 500 CYS B 566 CB CYS B 566 SG 0.152
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 566 CA - CB - SG ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 454 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 454 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 491 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA B 362 -129.79 77.58
REMARK 500 VAL B 542 -85.14 -47.03
REMARK 500 PRO B 597 26.37 -73.15
REMARK 500 ALA A 380 -55.67 -169.81
REMARK 500 LYS A 381 20.10 -74.35
REMARK 500 SER A 550 -69.69 -96.51
REMARK 500 PRO A 597 27.44 -70.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KZI RELATED DB: PDB
REMARK 900 RELATED ID: 4KZJ RELATED DB: PDB
REMARK 900 RELATED ID: 4JGV RELATED DB: PDB
DBREF 4KZM B 351 598 UNP P22736 NR4A1_HUMAN 351 598
DBREF 4KZM A 351 598 UNP P22736 NR4A1_HUMAN 351 598
SEQADV 4KZM MET B 350 UNP P22736 EXPRESSION TAG
SEQADV 4KZM ALA B 553 UNP P22736 SER 553 ENGINEERED MUTATION
SEQADV 4KZM LEU B 599 UNP P22736 EXPRESSION TAG
SEQADV 4KZM GLU B 600 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS B 601 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS B 602 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS B 603 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS B 604 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS B 605 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS B 606 UNP P22736 EXPRESSION TAG
SEQADV 4KZM MET A 350 UNP P22736 EXPRESSION TAG
SEQADV 4KZM ALA A 553 UNP P22736 SER 553 ENGINEERED MUTATION
SEQADV 4KZM LEU A 599 UNP P22736 EXPRESSION TAG
SEQADV 4KZM GLU A 600 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS A 601 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS A 602 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS A 603 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS A 604 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS A 605 UNP P22736 EXPRESSION TAG
SEQADV 4KZM HIS A 606 UNP P22736 EXPRESSION TAG
SEQRES 1 B 257 MET SER LYS PRO LYS GLN PRO PRO ASP ALA SER PRO ALA
SEQRES 2 B 257 ASN LEU LEU THR SER LEU VAL ARG ALA HIS LEU ASP SER
SEQRES 3 B 257 GLY PRO SER THR ALA LYS LEU ASP TYR SER LYS PHE GLN
SEQRES 4 B 257 GLU LEU VAL LEU PRO HIS PHE GLY LYS GLU ASP ALA GLY
SEQRES 5 B 257 ASP VAL GLN GLN PHE TYR ASP LEU LEU SER GLY SER LEU
SEQRES 6 B 257 GLU VAL ILE ARG LYS TRP ALA GLU LYS ILE PRO GLY PHE
SEQRES 7 B 257 ALA GLU LEU SER PRO ALA ASP GLN ASP LEU LEU LEU GLU
SEQRES 8 B 257 SER ALA PHE LEU GLU LEU PHE ILE LEU ARG LEU ALA TYR
SEQRES 9 B 257 ARG SER LYS PRO GLY GLU GLY LYS LEU ILE PHE CYS SER
SEQRES 10 B 257 GLY LEU VAL LEU HIS ARG LEU GLN CYS ALA ARG GLY PHE
SEQRES 11 B 257 GLY ASP TRP ILE ASP SER ILE LEU ALA PHE SER ARG SER
SEQRES 12 B 257 LEU HIS SER LEU LEU VAL ASP VAL PRO ALA PHE ALA CYS
SEQRES 13 B 257 LEU SER ALA LEU VAL LEU ILE THR ASP ARG HIS GLY LEU
SEQRES 14 B 257 GLN GLU PRO ARG ARG VAL GLU GLU LEU GLN ASN ARG ILE
SEQRES 15 B 257 ALA SER CYS LEU LYS GLU HIS VAL ALA ALA VAL ALA GLY
SEQRES 16 B 257 GLU PRO GLN PRO ALA SER CYS LEU ALA ARG LEU LEU GLY
SEQRES 17 B 257 LYS LEU PRO GLU LEU ARG THR LEU CYS THR GLN GLY LEU
SEQRES 18 B 257 GLN ARG ILE PHE TYR LEU LYS LEU GLU ASP LEU VAL PRO
SEQRES 19 B 257 PRO PRO PRO ILE ILE ASP LYS ILE PHE MET ASP THR LEU
SEQRES 20 B 257 PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 A 257 MET SER LYS PRO LYS GLN PRO PRO ASP ALA SER PRO ALA
SEQRES 2 A 257 ASN LEU LEU THR SER LEU VAL ARG ALA HIS LEU ASP SER
SEQRES 3 A 257 GLY PRO SER THR ALA LYS LEU ASP TYR SER LYS PHE GLN
SEQRES 4 A 257 GLU LEU VAL LEU PRO HIS PHE GLY LYS GLU ASP ALA GLY
SEQRES 5 A 257 ASP VAL GLN GLN PHE TYR ASP LEU LEU SER GLY SER LEU
SEQRES 6 A 257 GLU VAL ILE ARG LYS TRP ALA GLU LYS ILE PRO GLY PHE
SEQRES 7 A 257 ALA GLU LEU SER PRO ALA ASP GLN ASP LEU LEU LEU GLU
SEQRES 8 A 257 SER ALA PHE LEU GLU LEU PHE ILE LEU ARG LEU ALA TYR
SEQRES 9 A 257 ARG SER LYS PRO GLY GLU GLY LYS LEU ILE PHE CYS SER
SEQRES 10 A 257 GLY LEU VAL LEU HIS ARG LEU GLN CYS ALA ARG GLY PHE
SEQRES 11 A 257 GLY ASP TRP ILE ASP SER ILE LEU ALA PHE SER ARG SER
SEQRES 12 A 257 LEU HIS SER LEU LEU VAL ASP VAL PRO ALA PHE ALA CYS
SEQRES 13 A 257 LEU SER ALA LEU VAL LEU ILE THR ASP ARG HIS GLY LEU
SEQRES 14 A 257 GLN GLU PRO ARG ARG VAL GLU GLU LEU GLN ASN ARG ILE
SEQRES 15 A 257 ALA SER CYS LEU LYS GLU HIS VAL ALA ALA VAL ALA GLY
SEQRES 16 A 257 GLU PRO GLN PRO ALA SER CYS LEU ALA ARG LEU LEU GLY
SEQRES 17 A 257 LYS LEU PRO GLU LEU ARG THR LEU CYS THR GLN GLY LEU
SEQRES 18 A 257 GLN ARG ILE PHE TYR LEU LYS LEU GLU ASP LEU VAL PRO
SEQRES 19 A 257 PRO PRO PRO ILE ILE ASP LYS ILE PHE MET ASP THR LEU
SEQRES 20 A 257 PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL B 701 6
HET GOL A 701 6
HET GOL A 702 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 HOH *152(H2 O)
HELIX 1 1 ALA B 362 SER B 375 1 14
HELIX 2 2 SER B 378 LEU B 382 5 5
HELIX 3 3 ASP B 399 SER B 413 1 15
HELIX 4 4 SER B 413 LYS B 423 1 11
HELIX 5 5 GLY B 426 LEU B 430 5 5
HELIX 6 6 SER B 431 SER B 455 1 25
HELIX 7 7 LYS B 456 GLU B 459 5 4
HELIX 8 8 ARG B 472 GLY B 480 1 9
HELIX 9 9 ASP B 481 LEU B 496 1 16
HELIX 10 10 ASP B 499 ILE B 512 1 14
HELIX 11 11 GLU B 520 ALA B 543 1 24
HELIX 12 12 SER B 550 GLY B 557 1 8
HELIX 13 13 GLY B 557 ASP B 580 1 24
HELIX 14 14 PRO B 585 THR B 595 1 11
HELIX 15 15 ASN A 363 SER A 375 1 13
HELIX 16 16 ASP A 399 LYS A 423 1 25
HELIX 17 17 GLY A 426 LEU A 430 5 5
HELIX 18 18 SER A 431 SER A 455 1 25
HELIX 19 19 LYS A 456 GLU A 459 5 4
HELIX 20 20 ARG A 472 GLY A 480 1 9
HELIX 21 21 ASP A 481 LEU A 496 1 16
HELIX 22 22 ASP A 499 ILE A 512 1 14
HELIX 23 23 GLU A 520 GLY A 544 1 25
HELIX 24 24 SER A 550 GLY A 557 1 8
HELIX 25 25 LYS A 558 ASP A 580 1 23
HELIX 26 26 PRO A 585 LEU A 596 1 12
SHEET 1 A 2 LYS B 461 ILE B 463 0
SHEET 2 A 2 VAL B 469 HIS B 471 -1 O LEU B 470 N LEU B 462
SHEET 1 B 2 LYS A 461 ILE A 463 0
SHEET 2 B 2 VAL A 469 HIS A 471 -1 O LEU A 470 N LEU A 462
CISPEP 1 PRO B 361 ALA B 362 0 2.34
SITE 1 AC1 8 HIS B 372 SER B 375 GLY B 376 ARG B 450
SITE 2 AC1 8 ARG B 454 HOH B 813 HOH B 830 HOH B 832
SITE 1 AC2 2 LEU A 509 HOH A 860
SITE 1 AC3 10 HIS A 372 SER A 375 GLY A 376 PRO A 377
SITE 2 AC3 10 ARG A 450 ARG A 454 HOH A 832 HOH A 834
SITE 3 AC3 10 HOH A 877 HOH A 889
CRYST1 74.481 76.345 128.443 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013426 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013098 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END